PandemieGrippaleV1, PubMed, Curation, bibRecord, 000539

1918 Influenza receptor binding domain variants bind and replicate in primary human airway cells regardless of receptor specificity.

Identifieur interne : 000539 ( PubMed/Curation ); précédent : 000538; suivant : 000540

1918 Influenza receptor binding domain variants bind and replicate in primary human airway cells regardless of receptor specificity.

Auteurs : A Sally Davis [États-Unis] ; Daniel S. Chertow [États-Unis] ; Jason Kindrachuk [États-Unis] ; Li Qi [États-Unis] ; Louis M. Schwartzman [États-Unis] ; Jon Suzich [États-Unis] ; Sara Alsaaty [États-Unis] ; Carolea Logun [États-Unis] ; James H. Shelhamer [États-Unis] ; Jeffery K. Taubenberger [États-Unis]

Source :

Virology [ 1096-0341 ] ; 2016.

RBID : pubmed:27062579

Descripteurs français

KwdFr :
- Acide N-acétyl-neuraminique (métabolisme), Attachement viral, Bronches (cytologie), Cellules épithéliales (virologie), Pandémie de grippe de 1918-1919, Réaction de polymérisation en chaine en temps réel, Récepteurs viraux (métabolisme), Réplication virale, Sites de fixation, Sous-type H1N1 du virus de la grippe A (métabolisme), Trachée (cytologie).
MESH :
- cytologie : Bronches, Trachée.
- métabolisme : Acide N-acétyl-neuraminique, Récepteurs viraux, Sous-type H1N1 du virus de la grippe A.
- virologie : Cellules épithéliales.
- Attachement viral, Pandémie de grippe de 1918-1919, Réaction de polymérisation en chaine en temps réel, Réplication virale, Sites de fixation.

English descriptors

KwdEn :
- Binding Sites, Bronchi (cytology), Epithelial Cells (virology), Influenza A Virus, H1N1 Subtype (metabolism), Influenza Pandemic, 1918-1919, N-Acetylneuraminic Acid (metabolism), Real-Time Polymerase Chain Reaction, Receptors, Virus (metabolism), Trachea (cytology), Virus Attachment, Virus Replication.
MESH :
- chemical , metabolism : N-Acetylneuraminic Acid, Receptors, Virus.
- cytology : Bronchi, Trachea.
- metabolism : Influenza A Virus, H1N1 Subtype.
- virology : Epithelial Cells.
- Binding Sites, Influenza Pandemic, 1918-1919, Real-Time Polymerase Chain Reaction, Virus Attachment, Virus Replication.

Abstract

The 1918 influenza pandemic caused ~50 million deaths. Many questions remain regarding the origin, pathogenicity, and mechanisms of human adaptation of this virus. Avian-adapted influenza A viruses preferentially bind α2,3-linked sialic acids (Sia) while human-adapted viruses preferentially bind α2,6-linked Sia. A change in Sia preference from α2,3 to α2,6 is thought to be a requirement for human adaptation of avian influenza viruses. Autopsy data from 1918 cases, however, suggest that factors other than Sia preference played a role in viral binding and entry to human airway cells. Here, we evaluated binding and entry of five 1918 influenza receptor binding domain variants in a primary human airway cell model along with control avian and human influenza viruses. We observed that all five variants bound and entered cells efficiently and that Sia preference did not predict entry of influenza A virus to primary human airway cells evaluated in this model.

DOI: 10.1016/j.virol.2016.03.025
PubMed: 27062579

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Le document en format XML

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<country xml:lang="fr">États-Unis</country>
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</affiliation>
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<country xml:lang="fr">États-Unis</country>
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<term>Bronchi (cytology)</term>
<term>Epithelial Cells (virology)</term>
<term>Influenza A Virus, H1N1 Subtype (metabolism)</term>
<term>Influenza Pandemic, 1918-1919</term>
<term>N-Acetylneuraminic Acid (metabolism)</term>
<term>Real-Time Polymerase Chain Reaction</term>
<term>Receptors, Virus (metabolism)</term>
<term>Trachea (cytology)</term>
<term>Virus Attachment</term>
<term>Virus Replication</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acide N-acétyl-neuraminique (métabolisme)</term>
<term>Attachement viral</term>
<term>Bronches (cytologie)</term>
<term>Cellules épithéliales (virologie)</term>
<term>Pandémie de grippe de 1918-1919</term>
<term>Réaction de polymérisation en chaine en temps réel</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Réplication virale</term>
<term>Sites de fixation</term>
<term>Sous-type H1N1 du virus de la grippe A (métabolisme)</term>
<term>Trachée (cytologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>N-Acetylneuraminic Acid</term>
<term>Receptors, Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Bronches</term>
<term>Trachée</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Bronchi</term>
<term>Trachea</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide N-acétyl-neuraminique</term>
<term>Récepteurs viraux</term>
<term>Sous-type H1N1 du virus de la grippe A</term>
</keywords>
<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Cellules épithéliales</term>
</keywords>
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</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Influenza Pandemic, 1918-1919</term>
<term>Real-Time Polymerase Chain Reaction</term>
<term>Virus Attachment</term>
<term>Virus Replication</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Attachement viral</term>
<term>Pandémie de grippe de 1918-1919</term>
<term>Réaction de polymérisation en chaine en temps réel</term>
<term>Réplication virale</term>
<term>Sites de fixation</term>
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<front><div type="abstract" xml:lang="en">The 1918 influenza pandemic caused ~50 million deaths. Many questions remain regarding the origin, pathogenicity, and mechanisms of human adaptation of this virus. Avian-adapted influenza A viruses preferentially bind α2,3-linked sialic acids (Sia) while human-adapted viruses preferentially bind α2,6-linked Sia. A change in Sia preference from α2,3 to α2,6 is thought to be a requirement for human adaptation of avian influenza viruses. Autopsy data from 1918 cases, however, suggest that factors other than Sia preference played a role in viral binding and entry to human airway cells. Here, we evaluated binding and entry of five 1918 influenza receptor binding domain variants in a primary human airway cell model along with control avian and human influenza viruses. We observed that all five variants bound and entered cells efficiently and that Sia preference did not predict entry of influenza A virus to primary human airway cells evaluated in this model.</div>
</front>
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<DateCompleted><Year>2017</Year>
<Month>05</Month>
<Day>09</Day>
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<DateRevised><Year>2019</Year>
<Month>10</Month>
<Day>08</Day>
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<PubDate><Year>2016</Year>
<Month>06</Month>
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<Title>Virology</Title>
<ISOAbbreviation>Virology</ISOAbbreviation>
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<ArticleTitle>1918 Influenza receptor binding domain variants bind and replicate in primary human airway cells regardless of receptor specificity.</ArticleTitle>
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<Abstract><AbstractText>The 1918 influenza pandemic caused ~50 million deaths. Many questions remain regarding the origin, pathogenicity, and mechanisms of human adaptation of this virus. Avian-adapted influenza A viruses preferentially bind α2,3-linked sialic acids (Sia) while human-adapted viruses preferentially bind α2,6-linked Sia. A change in Sia preference from α2,3 to α2,6 is thought to be a requirement for human adaptation of avian influenza viruses. Autopsy data from 1918 cases, however, suggest that factors other than Sia preference played a role in viral binding and entry to human airway cells. Here, we evaluated binding and entry of five 1918 influenza receptor binding domain variants in a primary human airway cell model along with control avian and human influenza viruses. We observed that all five variants bound and entered cells efficiently and that Sia preference did not predict entry of influenza A virus to primary human airway cells evaluated in this model.</AbstractText>
<CopyrightInformation>Published by Elsevier Inc.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Davis</LastName>
<ForeName>A Sally</ForeName>
<Initials>AS</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis and Evolution Section, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, United States; Diagnostic Medicine and Pathobiology, Kansas State University College of Veterinary Medicine, Manhattan, KS, United States.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chertow</LastName>
<ForeName>Daniel S</ForeName>
<Initials>DS</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis and Evolution Section, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, United States; Critical Care Medicine Department, Clinical Center, NIH, Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Kindrachuk</LastName>
<ForeName>Jason</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Critical Care Medicine Department, Clinical Center, NIH, Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Qi</LastName>
<ForeName>Li</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis and Evolution Section, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Schwartzman</LastName>
<ForeName>Louis M</ForeName>
<Initials>LM</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis and Evolution Section, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Suzich</LastName>
<ForeName>Jon</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis and Evolution Section, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, United States; Critical Care Medicine Department, Clinical Center, NIH, Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Alsaaty</LastName>
<ForeName>Sara</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Critical Care Medicine Department, Clinical Center, NIH, Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Logun</LastName>
<ForeName>Carolea</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Critical Care Medicine Department, Clinical Center, NIH, Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shelhamer</LastName>
<ForeName>James H</ForeName>
<Initials>JH</Initials>
<AffiliationInfo><Affiliation>Critical Care Medicine Department, Clinical Center, NIH, Bethesda, MD, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Taubenberger</LastName>
<ForeName>Jeffery K</ForeName>
<Initials>JK</Initials>
<AffiliationInfo><Affiliation>Viral Pathogenesis and Evolution Section, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, United States. Electronic address: taubenbergerj@niaid.nih.gov.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>ZIA AI000986-10</GrantID>
<Agency>Intramural NIH HHS</Agency>
<Country>United States</Country>
</Grant>
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1918 Influenza receptor binding domain variants bind and replicate in primary human airway cells regardless of receptor specificity.

1918 Influenza receptor binding domain variants bind and replicate in primary human airway cells regardless of receptor specificity.

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